RT09_YEAST
ID RT09_YEAST Reviewed; 278 AA.
AC P38120; D6VQE1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=37S ribosomal protein S9, mitochondrial;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS9m {ECO:0000303|PubMed:28154081};
DE Flags: Precursor;
GN Name=MRPS9; OrderedLocusNames=YBR146W; ORFNames=YBR1123;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8536310; DOI=10.1007/bf00311878;
RA Koetter P., Entian K.-D.;
RT "Cloning and analysis of the nuclear gene MRP-S9 encoding mitochondrial
RT ribosomal protein S9 of Saccharomyces cerevisiae.";
RL Curr. Genet. 28:26-31(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11278769; DOI=10.1074/jbc.m010864200;
RA Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A.,
RA Jacquier A.;
RT "Identification of 12 new yeast mitochondrial ribosomal proteins including
RT 6 that have no prokaryotic homologues.";
RL J. Biol. Chem. 276:15861-15867(2001).
RN [5]
RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL SMALL COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x;
RA Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.;
RT "Tag-mediated isolation of yeast mitochondrial ribosome and mass
RT spectrometric identification of its new components.";
RL Eur. J. Biochem. 269:5203-5214(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND SUBUNIT.
RX PubMed=28154081; DOI=10.1126/science.aal2415;
RA Desai N., Brown A., Amunts A., Ramakrishnan V.;
RT "The structure of the yeast mitochondrial ribosome.";
RL Science 355:528-531(2017).
CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC mitochondrial genome-encoded proteins, including at least some of the
CC essential transmembrane subunits of the mitochondrial respiratory
CC chain. The mitoribosomes are attached to the mitochondrial inner
CC membrane and translation products are cotranslationally integrated into
CC the membrane. {ECO:0000305|PubMed:25609543,
CC ECO:0000305|PubMed:28154081}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S)
CC and a large (54S) subunit. The 37S small subunit contains a 15S
CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large
CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins.
CC {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:12392552,
CC ECO:0000269|PubMed:28154081}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}.
CC Note=Mitoribosomes are tethered to the mitochondrial inner membrane and
CC spatially aligned with the membrane insertion machinery through two
CC distinct membrane contact sites, formed by the 21S rRNA expansion
CC segment 96-ES1 and the inner membrane protein MBA1.
CC {ECO:0000269|PubMed:25609543}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000305}.
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DR EMBL; Z36015; CAA85104.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07261.1; -; Genomic_DNA.
DR PIR; S46017; S46017.
DR RefSeq; NP_009704.1; NM_001178494.1.
DR PDB; 5MRC; EM; 3.25 A; II=35-278.
DR PDB; 5MRE; EM; 3.75 A; II=35-278.
DR PDB; 5MRF; EM; 4.97 A; II=35-278.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P38120; -.
DR SMR; P38120; -.
DR BioGRID; 32845; 57.
DR ComplexPortal; CPX-1603; 37S mitochondrial small ribosomal subunit.
DR DIP; DIP-4924N; -.
DR IntAct; P38120; 9.
DR MINT; P38120; -.
DR STRING; 4932.YBR146W; -.
DR MaxQB; P38120; -.
DR PaxDb; P38120; -.
DR PRIDE; P38120; -.
DR EnsemblFungi; YBR146W_mRNA; YBR146W; YBR146W.
DR GeneID; 852443; -.
DR KEGG; sce:YBR146W; -.
DR SGD; S000000350; MRPS9.
DR VEuPathDB; FungiDB:YBR146W; -.
DR eggNOG; KOG1697; Eukaryota.
DR GeneTree; ENSGT00390000011204; -.
DR HOGENOM; CLU_036531_0_0_1; -.
DR InParanoid; P38120; -.
DR OMA; RMDKYNV; -.
DR BioCyc; YEAST:G3O-29098-MON; -.
DR PRO; PR:P38120; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38120; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..10
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 11..278
FT /note="37S ribosomal protein S9, mitochondrial"
FT /id="PRO_0000030653"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..278
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 31925 MW; 71B2028E39D2723C CRC64;
MFSRLSLFRR AALAPAPMRM SFRTIYQKTE DELPRRIVPK LATFYSANPN HEDRINRLER
LLRKYIKLPS QNNNEAQQTK APWISFDEYA LIGGGTKLKP TQYTQLLYML NKLHNIDPQL
TNDEITSELS QYYKKSSMLS NNIKIKTLDE FGRSIAVGKR KSSTAKVFVV RGTGEILVNG
RQLNDYFLKM KDRESIMYPL QVIESVGKYN IFATTSGGGP TGQAESIMHA IAKALVVFNP
LLKSRLHKAG VLTRDYRHVE RKKPGKKKAR KMPTWVKR
